MolNFT v1 · #143187 · protein
Filamentous assembly of green fluorescent protein supported by a C- terminal fusion of 18-residues, viewed in space group P212121 form 2
6AS9: “Filamentous assembly of green fluorescent protein supported by a C- terminal fusion of 18-residues, viewed in…”. X-ray diffraction, 1 ligand (PIA), 1 pocket (best druggability 0.74). MolNFT v1 #143187 on GenesisL1: 3D structure…
- PDB
- 6AS9
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein
- UniProt
- P42212
- Ligands
- PIA
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Green fluorescent protein | protein | 244 | 18% helix, 48% strand | P42212 |
Ligands and binding sites
- PIA · [(4Z)-2-[(1S)-1-aminoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.74 | 0.98 | 22 | PIA |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6AS9 · Filamentous Assembly of Green Fluorescent Protein Supported by a C-terminal fusion of… · the same entry in another collection · chain A against A, TM-score 1.00
- P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P42212
- Elsewhere: RCSB PDB 6AS9 · PDBe 6AS9 · UniProt P42212
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